Mitochondrial complex III Rieske Fe-S protein processing and assembly

Fernández-Vizarra, Erika; Zeviani, Massimo

doi:10.1080/15384101.2017.1417707

Cited by 65 publications

(62 citation statements)

References 67 publications

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“…In this work, we not only showed the significance of FTSH4 for the biogenesis of complexes I and V in germinating seeds, but we additionally revealed for the first time the importance of this protease in the biogenesis of complexes II, III, and IV. Concerning complex III, in the ftsh4 seeds we detected a decreased abundance of RIESKE, the iron-sulfur protein essential for maturation of this complex (Fernandez-Vizarra and Zeviani, 2017 ). It is noteworthy that a dramatic reduction in the abundance of the RIESKE peptides was observed in WT and ftsh4 seeds at the last studied stage (42 h), however, the mechanism behind this process is unknown.…”

Section: Discussionmentioning

confidence: 98%

Targeted Proteomics Approach Toward Understanding the Role of the Mitochondrial Protease FTSH4 in the Biogenesis of OXPHOS During Arabidopsis Seed Germination

et al. 2018

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Seed germination provides an excellent model to study the process of mitochondrial biogenesis. It is a complex and strictly regulated process which requires a proper biogenesis of fully active organelles from existing promitochondrial structures. We have previously reported that the lack of the inner mitochondrial membrane protease FTSH4 delayed Arabidopsis seed germination. Here, we implemented a targeted mass spectrometry-based approach, Multiple Reaction Monitoring (MRM), with stable-isotope-labeled standard peptides for increased sensitivity, to quantify mitochondrial proteins in dry and germinating wild-type and ftsh4 mutant seeds, lacking the FTSH4 protease. Using total seed protein extracts we measured the abundance of the peptide targets belonging to the OXPHOS complexes, AOX1A, transport, and inner membrane scaffold as well as mitochondrial proteins that are highly specific to dry and germinating seeds. The MRM assay showed that the abundance of these proteins in ftsh4 did not differ substantially from that observed in wild-type at the level of dry seed and after stratification, but we observed a reduction in protein abundance in most of the examined OXPHOS subunits in the later stages of germination. These changes in OXPHOS protein levels in ftsh4 mutants were accompanied by a lower cytochrome pathway activity as well as an increased AOX1A amount at the transcript and protein level and alternative pathway activity. The analyses of the steady-state transcript levels of mitochondrial and nuclear genes encoding OXPHOS subunits did not show significant difference in their amount, indicating that the observed changes in the OXPHOS occurred at the post-transcriptional level. At the time when ftsh4 seeds were fully germinated, the abundance of the OXPHOS proteins in the mutant was either slightly lowered or comparable to these amounts in wild-type seeds at the similar developmental stage. By the implementation of an integrative approach combining targeted proteomics, quantitative transcriptomics, and physiological studies we have shown that the FTSH4 protease has an important role in the biogenesis of OXPHOS and thus biogenesis of mitochondria during germination of Arabidopsis seeds.

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Section: Discussionmentioning

confidence: 98%

Targeted Proteomics Approach Toward Understanding the Role of the Mitochondrial Protease FTSH4 in the Biogenesis of OXPHOS During Arabidopsis Seed Germination

et al. 2018

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“…Structurally, it is a tightly bound symmetrical dimer (cIII 2 ), being each ‘monomer’ composed of three catalytic core (MT-CYB, CYC1 and UQCRFS1) and seven supernumerary subunits [ 81 , 82 ]. The 78-amino acid mitochondrial targeting sequence (MTS) cleaved off from UQCRFS1 was considered an extra subunit [ 81 , 83 ], but it needs to be cleared out to maintain cIII 2 structural and functional fitness [ 84 , 85 ]. MT-CYB contains two b -type haems with different redox potential as well as two CoQ binding sites.…”

Section: Assembly Of Complex IIImentioning

confidence: 99%

Assembly of mammalian oxidative phosphorylation complexes I–V and supercomplexes

Signes

Fernández-Vizarra

2018

Essays in Biochemistry

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220

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The assembly of the five oxidative phosphorylation system (OXPHOS) complexes in the inner mitochondrial membrane is an intricate process. The human enzymes comprise core proteins, performing the catalytic activities, and a large number of ‘supernumerary’ subunits that play essential roles in assembly, regulation and stability. The correct addition of prosthetic groups as well as chaperoning and incorporation of the structural components require a large number of factors, many of which have been found mutated in cases of mitochondrial disease. Nowadays, the mechanisms of assembly for each of the individual complexes are almost completely understood and the knowledge about the assembly factors involved is constantly increasing. On the other hand, it is now well established that complexes I, III and IV interact with each other, forming the so-called respiratory supercomplexes or ‘respirasomes’, although the pathways that lead to their formation are still not completely clear. This review is a summary of our current knowledge concerning the assembly of complexes I–V and of the supercomplexes.

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“…turnover in response to stress or metabolic stimuli [122,388]. Hence, the mishandling of oxidative or metabolic stress could play a role in the pathogenesis of the disease.…”

Section: Accepted Articlementioning

confidence: 99%

Mitochondrial disorders of the OXPHOS system

2020

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Mitochondrial disorders are amongst the most frequent inborn errors of metabolism, their primary cause being the dysfunction of the oxidative phosphorylation system (OXPHOS). OXPHOS is composed of the electron transport chain (ETC), formed by four multimeric enzymes and two mobile electron carriers, plus an ATP synthase (also called complex V). The ETC performs the redox reactions involved in cellular respiration while generating the proton motive force used by complex V to synthesize ATP. OXPHOS biogenesis involves multiple steps, starting from the expression of genes encoded in physically separated genomes, namely the mitochondrial and nuclear DNA, to the coordinated assembly of components and cofactors building each individual complex and eventually the supercomplexes. The genetic cause underlying around half of the diagnosed mitochondrial disease cases is currently known. Many of these cases result from pathogenic variants in genes encoding structural subunits or additional factors directly involved in the assembly of the ETC complexes. Here we review the historical and most recent findings concerning the clinical phenotypes and the molecular pathological mechanisms underlying this particular group of disorders.

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Mitochondrial complex III Rieske Fe-S protein processing and assembly

Cited by 65 publications

References 67 publications

Targeted Proteomics Approach Toward Understanding the Role of the Mitochondrial Protease FTSH4 in the Biogenesis of OXPHOS During Arabidopsis Seed Germination

Targeted Proteomics Approach Toward Understanding the Role of the Mitochondrial Protease FTSH4 in the Biogenesis of OXPHOS During Arabidopsis Seed Germination

Assembly of mammalian oxidative phosphorylation complexes I–V and supercomplexes

Mitochondrial disorders of the OXPHOS system

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